Engineered alcohol oxidases catalyse transesterification in aqueous media without competing hydrolysis
Transesterification reactions are fundamental transformations in organic chemistry, yet performing them in aqueous media is challenging because of the competing hydrolysis reaction. In this study, we describe a mutant of alcohol oxidase from Phanerochaete chrysosporium (PcAOx-VPN) that also exhibits transesterification activity. Moreover, PcAOx-VPN displays no detectable hydrolytic activity, owing to its hydrophobic active site, which effectively excludes water. These characteristics make PcAOx-VPN a promising catalyst for transesterification reactions in aqueous media, a context that is typically compromised by competing hydrolysis.
Authors
- Chenhao Feng
- Bin Wu (ORCID: https://orcid.org/0000-0002-4722-4226)
- Chiara Domestici (ORCID: https://orcid.org/0000-0003-3128-4600)
- Ulf Hanefeld (ORCID: https://orcid.org/0000-0002-4102-6165)
- Yunjian Ma (ORCID: https://orcid.org/0000-0001-8003-8233)
- Thomas Hilberath (ORCID: https://orcid.org/0000-0002-9778-2509)
- Evgeny A. Pidko (ORCID: https://orcid.org/0000-0001-9242-9901)
- Yuxuan Wang (ORCID: https://orcid.org/0000-0002-1649-6974)
- Limei Ren
- Frank Hollmann
Institutions
- Shijiazhuang University (CN)
- Guangdong Institute of Intelligent Manufacturing (CN)
- South China University of Technology (CN)
- Hebei GEO University (CN)
- Delft University of Technology (NL)
Publication Details
- Journal
- Nature Communications
- Published
- 2026-01-30
- DOI
- https://doi.org/10.1038/s41467-026-68899-y
- Primary Topic
- Enzyme Catalysis and Immobilization
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- European Commission
- National Natural Science Foundation of China